Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyGlyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase 8034905 3000739 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyGlyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase 8034905 3000739 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AGlyoxalase_1e1qinA2 A: a+b two layersX: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenaseF: Glyoxalase_1ECOD (1.6)
AGlyoxalase_6e1qinA1 A: a+b two layersX: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenaseF: Glyoxalase_6ECOD (1.6)
BGlyoxalase_1e1qinB2 A: a+b two layersX: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenaseF: Glyoxalase_1ECOD (1.6)
BGlyoxalase_6e1qinB1 A: a+b two layersX: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenaseF: Glyoxalase_6ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.10.180.10 Alpha Beta Roll 2,3-Dihydroxybiphenyl 1,2-Dioxygenase domain 1CATH (4.3.0)
B3.10.180.10 Alpha Beta Roll 2,3-Dihydroxybiphenyl 1,2-Dioxygenase domain 1CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF00903Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily (Glyoxalase)Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily- Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B
PROTEIN (LACTOYLGLUTATHIONE LYASE)

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
A, B
lactoylglutathione lyase  M-CSA #32

Lactoyl-glutathione lyase (or glyoxalase I) is part of the glyoxalase system which catalyses the conversion of acyclic alpha-oxoaldehydes into the corresponding alpha-hydroxyacids. Glyoxalase I catalyses the isomerization of the hemithioacetal (formed spontaneously from alpha-oxoaldehyde and GSH), to S-2-hydroxyacylglutathione (or R) derivatives, therefore decreasing the steady-state concentrations of physiological alpha-oxoaldehydes and associated glycation reactions. Physiological substrates of glyoxalase I are methylglyoxal, glyoxal and other acyclic alpha-oxoaldehydes.

This is the first of two steps in the conversion of 2-oxo-aldehydes to the corresponding 2-hydroxycarboxylic acids by way of the glyoxylase system. Methylglyoxal is produced as a by product of the triosephosphate isomerase reaction in glycolysis and, if not removed, is toxic as it reacts readily with with proteins and nucleic acids.

Defined by 4 residues: GLN:A-33GLU:A-99HIS:B-126GLU:B-172
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